Browse by MACROMOLECULE type: protein

SASDCU9 – Bacteriophage phi-X174 - Before Reaction with LPS

Bacteriophage phi-X174 experimental SAS data
Bacteriophage phi-X174 Kratky plot
Sample: Bacteriophage phi-X174 monomer, 0 kDa protein
Buffer: 0.06 M NH4Cl2, 0.09 M NaCl, 0.1 M KCl, 1 mM MgS04, 1 mM CaCl2, 0.1 M Tris-HCl, pH: 7.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 25
Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls. Proc Natl Acad Sci U S A 114(52):13708-13713 (2017)
Sun Y, Roznowski AP, Tokuda JM, Klose T, Mauney A, Pollack L, Fane BA, Rossmann MG
RgGuinier 12.1 nm

SASDCV9 – Bacteriophage phi-X174 - ~45s after mixing with LPS

Bacteriophage phi-X174 experimental SAS data
Bacteriophage phi-X174 Kratky plot
Sample: Bacteriophage phi-X174 monomer, 0 kDa protein
Buffer: 0.15 mg/mL LPS, 0.06 M NH4Cl2, 0.09 M NaCl, 0.1 M KCl, 1 mM MgS04, 1 mM CaCl2, 0.1 M Tris-HCl, pH: 7.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 25
Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls. Proc Natl Acad Sci U S A 114(52):13708-13713 (2017)
Sun Y, Roznowski AP, Tokuda JM, Klose T, Mauney A, Pollack L, Fane BA, Rossmann MG
RgGuinier 12.7 nm

SASDCW9 – Bacteriophage phi-X174 - ~245s after mixing with LPS

Bacteriophage phi-X174 experimental SAS data
Bacteriophage phi-X174 Kratky plot
Sample: Bacteriophage phi-X174 monomer, 0 kDa protein
Buffer: 0.15 mg/mL LPS, 0.06 M NH4Cl2, 0.09 M NaCl, 0.1 M KCl, 1 mM MgS04, 1 mM CaCl2, 0.1 M Tris-HCl, pH: 7.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 25
Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls. Proc Natl Acad Sci U S A 114(52):13708-13713 (2017)
Sun Y, Roznowski AP, Tokuda JM, Klose T, Mauney A, Pollack L, Fane BA, Rossmann MG
RgGuinier 12.9 nm

SASDCX9 – Bacteriophage phi-X174 - ~545s after mixing with LPS

Bacteriophage phi-X174 experimental SAS data
Bacteriophage phi-X174 Kratky plot
Sample: Bacteriophage phi-X174 monomer, 0 kDa protein
Buffer: 0.15 mg/mL LPS, 0.06 M NH4Cl2, 0.09 M NaCl, 0.1 M KCl, 1 mM MgS04, 1 mM CaCl2, 0.1 M Tris-HCl, pH: 7.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 25
Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls. Proc Natl Acad Sci U S A 114(52):13708-13713 (2017)
Sun Y, Roznowski AP, Tokuda JM, Klose T, Mauney A, Pollack L, Fane BA, Rossmann MG
RgGuinier 12.9 nm

SASDBY4 – Pentameric Nucleoplasmin-histone H2A/H2B complex

Nucleoplasmin core + A2Histone H2A (ΔAla127)Histone H2B 1.1 (Ser33Thr) experimental SAS data
DAMFILT model
Sample: Nucleoplasmin core + A2 pentamer, 81 kDa Xenopus laevis protein
Histone H2A (ΔAla127) pentamer, 69 kDa Xenopus laevis protein
Histone H2B 1.1 (Ser33Thr) pentamer, 67 kDa Xenopus laevis protein
Buffer: 20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTT, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2016 Jan 7
Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release. Nat Commun 8(1):2215 (2017)
Warren C, Matsui T, Karp JM, Onikubo T, Cahill S, Brenowitz M, Cowburn D, Girvin M, Shechter D
RgGuinier 4.4 nm
Dmax 14.0 nm
VolumePorod 402 nm3

SASDC26 – DH-PH - Dbl-homology domain (DH) and Pleckstrin-homology (PH) of Bcr-Abl tyrosine kinase p210

BCR-ABL p210 fusion protein (DH-PH) experimental SAS data
DH-PH - Dbl-homology domain (DH) and Pleckstrin-homology (PH) of Bcr-Abl tyrosine kinase p210 Rg histogram
Sample: BCR-ABL p210 fusion protein (DH-PH) monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Oct 13
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun 8(1):2101 (2017)
Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O
RgGuinier 3.2 nm
Dmax 11.1 nm
VolumePorod 69 nm3

SASDC36 – DH - Dbl-homology domain of Bcr-Abl tyrosine kinase p210

BCR-ABL p210 fusion protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: BCR-ABL p210 fusion protein monomer, 25 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Oct 13
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun 8(1):2101 (2017)
Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O
RgGuinier 2.1 nm
Dmax 7.3 nm
VolumePorod 38 nm3

SASDC46 – PH - Pleckstrin-homology domain of Bcr-Abl tyrosine kinase p210

BCR-ABL p210 fusion protein (PH domain) experimental SAS data
SREFLEX model
Sample: BCR-ABL p210 fusion protein (PH domain) monomer, 22 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Nov 10
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. Nat Commun 8(1):2101 (2017)
Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O
RgGuinier 2.0 nm
Dmax 6.6 nm
VolumePorod 38 nm3

SASDCB7 – Streptococcus pneumoniae phosphodiesterase Pde2

DHH subfamily 1 protein experimental SAS data
DHH subfamily 1 protein Kratky plot
Sample: DHH subfamily 1 protein dimer, 70 kDa Streptococcus pneumoniae serotype … protein
Buffer: 20mM Tris, 200 mM NaCl, 5%(v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 23
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.7 nm
Dmax 7.7 nm
VolumePorod 87 nm3

SASDCC7 – Thermotoga martitima phosphodiesterase TM1595 D80N D154N (inactive mutant)

T.maritima PDE experimental SAS data
T.maritima PDE Kratky plot
Sample: T.maritima PDE dimer, 76 kDa Thermotoga maritima protein
Buffer: 25mM Tris 500mM NaCl 3% (v/v) glycerol 2mM MgCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jun 17
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.8 nm
Dmax 7.9 nm
VolumePorod 115 nm3